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- PDB-1xlg: MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xlg | ||||||
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Title | MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT | ||||||
![]() | D-XYLOSE ISOMERASE | ||||||
![]() | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | ![]() xylose isomerase / D-xylose metabolic process / xylose isomerase activity / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Collyer, C.A. / Henrick, K. / Blow, D.M. | ||||||
![]() | ![]() Title: Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift. Authors: Collyer, C.A. / Henrick, K. / Blow, D.M. #1: ![]() Title: Observations of Reaction Intermediates and the Mechanism of Aldose-Ketose Interconversion by D-Xylose Isomerase Authors: Collyer, C.A. / Blow, D.M. #2: ![]() Title: Comparison of Backbone Structures of Glucose Isomerase from Streptomyces and Arthrobacter Authors: Henrick, K. / Blow, D.M. / Carrell, H.L. / Glusker, J.P. #3: ![]() Title: The Crystallization of Glucose Isomerase from Arthrobacter B3728 Authors: Akins, J. / Brick, P. / Jones, H.B. / Hirayama, N. / Shaw, P.-C. / Blow, D.M. | ||||||
History |
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Remark 700 | SHEET THE TWO SHEETS PRESENTED AS *BAA* AND *BAB* ON SHEET RECORDS BELOW ARE ACTUALLY EIGHT- ...SHEET THE TWO SHEETS PRESENTED AS *BAA* AND *BAB* ON SHEET RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. EACH IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 174.2 KB | Display | ![]() |
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PDB format | ![]() | 137.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 394.8 KB | Display | ![]() |
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Full document | ![]() | 422.5 KB | Display | |
Data in XML | ![]() | 19.5 KB | Display | |
Data in CIF | ![]() | 32.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1xlaC ![]() 1xlbC ![]() 1xlcC ![]() 1xldC ![]() 1xleC ![]() 1xlfC ![]() 1xlhC ![]() 1xliC ![]() 1xljC ![]() 1xlkC ![]() 1xllC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 186 AND PRO B 186 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 43209.168 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Sugar | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57.04 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Num. obs: 34465 / % possible obs: 98.4 % / Num. measured all: 70003 / Rmerge(I) obs: 0.086 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.5→10 Å Details: THIS IS MODEL(18) AS DESCRIBED IN THE JRNL RECORDS ABOVE. EACH OF THE TWO MONOMERS OF THE TETRAMER IN THE ASYMMETRIC UNIT HAVE ONE MG++, ONE AL+++, AND ONE D-XYLOSE/XYLULOSE BOUND AT PH 6.
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 25.6 Å2 |